ID A0A067FHB3_CITSI Unreviewed; 736 AA.
AC A0A067FHB3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=CISIN_1g003196mg {ECO:0000313|EMBL:KDO66774.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO66774.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO66774.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001275,
CC ECO:0000256|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; KK784898; KDO66774.1; -; Genomic_DNA.
DR EMBL; KK784898; KDO66775.1; -; Genomic_DNA.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468:SF4; ALPHA-GLUCAN PHOSPHORYLASE 2, CYTOSOLIC; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 686
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 736 AA; 83318 MW; 953F2D0D7C33B15A CRC64;
MADAKANGKN EAAKLAKIPA AANPLANEPS AIASNISYHV QYSPHFSPTK FEPEQAFFAT
AESVRDRLIQ QWNETYHHFN KVDPKQTYYL SMEFLQGRTL TNAIGSLDIQ NAYADALNNL
GHVLEEIAEQ EKDAALGNGG LGRLASCFLD SMATLNLPAW GYGLRYRYGL FKQKITKQGQ
EEVAEDWLEK FSPWEVVRHD VVFPVRFFGS VMVNPNGTRK WVGGEVVQAV AYDIPIPGYK
TKNTISLRLW DAKASAEDFN LFQFNDGQYE SAAQLHSRAQ QICAVLYPGD STEEGKLLRL
KQQFFLCSAS LQDMILRFKE RKSGRQWSEF PSKVAVQLND THPTLAIPEL MRLLMDEEGL
GWDEAWDITT RTVAYTNHTV LPEALEKWSQ AVMWKLLPRH MEIIEEIDKR FIAMVRSTRS
DLESKIPSMC ILDNNPKKPV VRMANLCVVS AHTVNGVAQL HSDILKADLF ADYVSLWPNK
LQNKTNGITP RRWLRFCNPE LSKIITKWLK TDQWVTNLDL LVGLRQFADN TELQAEWESA
KMASKKHLAD YIWRVTGVTI DPNSLFDIQV KRIHEYKRQL LNILGAIYRY KKLKEMSPQE
RKKTTPRTIM IGGKAFATYT NAKRIVKLVN DVGEVVNTDP EVNSYLKVVF VPNYNVSVAE
LLIPGSELSQ HISTAGMEAS GTSNMKFSLN GCLIIGTLDG ANVEIRQEIG EENFFLFGAV
AEQVPKLRKE REDGLV
//
